Recombinant Human AMD1 His Protein

Images

 
SDS-Page: Recombinant Human AMD1 His Protein [NBP1-98924] - 3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain

Product Details

Summary
Reactivity HuSpecies Glossary
Applications PAGE
Concentration
0.5 mg/ml

Order Details

Recombinant Human AMD1 His Protein Summary

Description
A recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 68-334 of Human AMD1

Source: E.coli

Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MGSHMSSMFV SKRRFILKTC GTTLLLKALV PLLKLARDYS GFDSIQSFFY SRKNFMKPSH QGYPHRNFQE EIEFLNAIFP NGAAYCMGRM NSDCWYLYTL DFPESRVISQ PDQTLEILMS ELDPAVMDQF YMKDGVTAKD VTRESGIRDL IPGSVIDATM FNPCGYSMNG MKSDGTYWTI HITPEPEFSY VSFETNLSQT SYDDLIRKVV EVFKPGKFVT TLFVNQSSKC RTVLASPQKI EGFKRLDCQS AMFNDYNFVF TSFAKKQQQQ QS

Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
AMD1
Purity
>80%, by SDS-PAGE

Applications/Dilutions

Dilutions
  • SDS-Page
Theoretical MW
33.3 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
20 mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1 M NaCl, 1 mM DTT
Preservative
No Preservative
Concentration
0.5 mg/ml
Purity
>80%, by SDS-PAGE

Alternate Names for Recombinant Human AMD1 His Protein

  • adenosylmethionine decarboxylase 1
  • AdoMetDC
  • AMD
  • AMD1
  • DKFZp313L1234
  • EC 4.1.1.50
  • S-adenosylmethionine decarboxylase 1
  • S-adenosylmethionine decarboxylase proenzyme
  • SAMDC
  • SAMDCFLJ26964

Background

AMD1, also known as adenosylmethionine decarboxylase proenzyme, is synthesized initially as an inactive proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. Recombinant human AMD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

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Bioinformatics

Gene Symbol AMD1